A7E300

SS
Gene name
DLC1 (ARHGAP7, STARD12)
Protein name
Rho GTPase-activating protein 7
Names
Deleted in liver cancer 1 protein homolog, DLC-1, Rho-type GTPase-activating protein 7, START domain-containing protein 12, StARD12, StAR-related lipid transfer protein 12
Species
Bos taurus (Bovine)
KEGG Pathway
bta:511433
EC number
Protein Class

Descriptions

DLC1 encodes a Rho GTPase-activating protein (RhoGAP) and negative regulator of specific Rho family proteins (RhoA-C and Cdc42). DLC1 is a multi-domain protein, with the RhoGAP catalytic domain flanked by an amino-terminal sterile motif (SAM) and a carboxyl-terminal START domain. In a study with human DLC1 isoform 1, truncation of SAM domain activates RhoGAP catalytic domain.

Autoinhibitory domains (AIDs)

37-104 (SAM domain) SS

Target domain

662-868 (Rho-GAP domain)

Relief mechanism

Cleavage

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for A7E300

Entry ID Method Resolution Chain Position Source
AF-A7E300-F1 Predicted AlphaFoldDB

No variants for A7E300

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A7E300

No associated diseases with A7E300

3 regional properties for A7E300

Type Name Position InterPro Accession
domain Rho GTPase-activating protein domain 662 - 868 IPR000198
domain Sterile alpha motif domain 43 - 102 IPR001660
domain START domain 898 - 1108 IPR002913

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cell junction, focal adhesion
  • Membrane ; Peripheral membrane protein
  • Colocalizes with EF1A1 at actin-rich regions in the cell periphery
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
focal adhesion A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ).
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

2 GO annotations of molecular function

Name Definition
GTPase activator activity Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP.
lipid binding Binding to a lipid.

2 GO annotations of biological process

Name Definition
regulation of Rho protein signal transduction Any process that modulates the frequency, rate or extent of Rho protein signal transduction.
signal transduction The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
B9VTT2 DLC1 Rho GTPase-activating protein 7 Canis lupus familiaris (Dog) (Canis familiaris) SS
Q9P2N2 ARHGAP28 Rho GTPase-activating protein 28 Homo sapiens (Human) PR
Q8BN58 Arhgap28 Rho GTPase-activating protein 28 Mus musculus (Mouse) PR
Q9R0Z9 Dlc1 Rho GTPase-activating protein 7 Mus musculus (Mouse) SS
Q63744 Dlc1 Rho GTPase-activating protein 7 Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MARPLRAPLR RSFSDHIRDS TARALDVIWK NTRDRRLAEI EAKEACDWLR AAGFPQYAQL
70 80 90 100 110 120
YEDLLFPIDI SSVKREHDFL DRDAIEALCR RLNTLNKCAV MKLEISPHRK RSEDSDEDEP
130 140 150 160 170 180
CAISGKWTFQ RDSKRWSRLE EFDVFSPKQD PIPGSPDAVH LKSAPSHENM QTDLSDRQEV
190 200 210 220 230 240
ASVHSTGSLT THAPQRGEAA PARTNSVLSV CSSGTFVGND DSFCSLPSPK ELSSFSFSMK
250 260 270 280 290 300
GHEKAAKSKT HSLLKRMESL KLKGSHHSKH KAPSKLGLII SGPILQEGVD EEKLKQLNCV
310 320 330 340 350 360
EISALNGNHI NVPMVRKRSI SSSTQTSSSS SQSETSSNVS TPSPVTRTRS LSACNKRGGM
370 380 390 400 410 420
YLEGFDPFNQ STFNNVMEQN CKNRESYPED TVFYIPEDHK PGTFPKALSN GSFSPSGNNS
430 440 450 460 470 480
SVNWRTGSFH GPGHISLRRE NSSPKELKRR NSSSSVSSRL SIYDNVPGSI LYSSSGDLAD
490 500 510 520 530 540
LENEDIFPEL DDILYHVKGM QRIVNQWSEK FSDEGDSDSA LDSVSPCPSS PKQIHLDVDN
550 560 570 580 590 600
DRATPSDLDS TGNSLNEPEE PSDIPERRDS GVGASLTRSN RHRLRWHSFQ SSHRPSLNSV
610 620 630 640 650 660
SLQINCQSVA QMNLLQKYSL LKLTALLEKY TPSNKHGFSW AVPKFMKRIK VPDYKDRNVF
670 680 690 700 710 720
GVPLTVNVQR TGQPLPQSIQ QAMRYLRNHC LDQVGLFRKS GVKSRIQALR QMNESTIDCV
730 740 750 760 770 780
NYEGQSAYDV ADMLKQYFRD LPEPLMTNKL SETFLQIYQY VPKDQRLQAI KAAIMLLPDE
790 800 810 820 830 840
NREVLQTLLY FLSDVTAAVK ENQMTPTNLA VCLAPSLFHL NTLKRENSSP RVMQRKQSLG
850 860 870 880 890 900
KPDQKDLNEN LAATQGLAHM IAECKKLFQV PEEMSRCRNS YTEQELKPLT LEALGRLCND
910 920 930 940 950 960
DSADYQHFLQ DCVDSLFKEV KEKFKGWVSY STSEQAELSY KKVSEGPPLR LWRATIEVPA
970 980 990 1000 1010 1020
TPEEILKRLL KEQHLWDVDL LDSKVIEILD SQTEIYQYVQ NSMAPHPARD YVVLRTWRTN
1030 1040 1050 1060 1070 1080
LPKGACALLL TSVDHDRAPV VGVRVNVLLA RYLIEPCGSG KSKLTYMCRA DLRGHMPEWY
1090 1100 1110
TKSFGHLCAA EVVKIRDSFS HQNTETKDTK SR